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Protein

Uridylate kinase

Gene

SPCC1795.05c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP.UniRule annotation

Catalytic activityi

ATP + UMP = ADP + UDP.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per monomer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391NMPUniRule annotation
Binding sitei98 – 981NMPUniRule annotation
Binding sitei129 – 1291ATPUniRule annotation
Binding sitei135 – 1351NMPUniRule annotation
Binding sitei146 – 1461NMPUniRule annotation
Binding sitei174 – 1741ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 176ATPUniRule annotation
Nucleotide bindingi61 – 633NMPUniRule annotation
Nucleotide bindingi91 – 944NMPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
Uridylate kinaseUniRule annotation (EC:2.7.4.14UniRule annotation)
Short name:
UKUniRule annotation
Alternative name(s):
ATP:UMP phosphotransferaseUniRule annotation
Deoxycytidylate kinaseUniRule annotation
Short name:
CKUniRule annotation
Short name:
dCMP kinaseUniRule annotation
Uridine monophosphate kinaseUniRule annotation
Short name:
UMP kinaseUniRule annotation
Short name:
UMPKUniRule annotation
Gene namesi
ORF Names:SPCC1795.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1795.05c.
PomBaseiSPCC1795.05c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191Uridylate kinasePRO_0000158946Add
BLAST

Proteomic databases

MaxQBiO59771.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi275517. 1 interaction.
MINTiMINT-4676056.

Structurei

3D structure databases

ProteinModelPortaliO59771.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6331NMPbindUniRule annotationAdd
BLAST
Regioni128 – 13811LIDUniRule annotationAdd
BLAST

Domaini

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.UniRule annotation

Sequence similaritiesi

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000238771.
InParanoidiO59771.
KOiK13800.
OMAiCANVVEH.
OrthoDBiEOG092C5OQU.
PhylomeDBiO59771.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03172. Adenylate_kinase_UMP_CMP_kin. 1 hit.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O59771-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYNVIFVLGG PGAGKGTQCD RLAEKFDKFV HISAGDCLRE EQNRPGSKYG
60 70 80 90 100
NLIKEYIKDG KIVPMEITIS LLETKMKECH DKGIDKFLID GFPREMDQCE
110 120 130 140 150
GFEKSVCPAK FALYFRCGQE TMLKRLIHRG KTSGRSDDNI ESIKKRFVTY
160 170 180 190
TKASMPVVEY LKSQNRLITI DAEQDPDAVF EDTVKALQPY L
Length:191
Mass (Da):21,716
Last modified:August 1, 1998 - v1
Checksum:iAD344378AC334757
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA18640.1.
PIRiT41138.
RefSeqiNP_588039.1. NM_001023031.2.

Genome annotation databases

EnsemblFungiiSPCC1795.05c.1; SPCC1795.05c.1:pep; SPCC1795.05c.
GeneIDi2538942.
KEGGispo:SPCC1795.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA18640.1.
PIRiT41138.
RefSeqiNP_588039.1. NM_001023031.2.

3D structure databases

ProteinModelPortaliO59771.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275517. 1 interaction.
MINTiMINT-4676056.

Proteomic databases

MaxQBiO59771.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1795.05c.1; SPCC1795.05c.1:pep; SPCC1795.05c.
GeneIDi2538942.
KEGGispo:SPCC1795.05c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1795.05c.
PomBaseiSPCC1795.05c.

Phylogenomic databases

HOGENOMiHOG000238771.
InParanoidiO59771.
KOiK13800.
OMAiCANVVEH.
OrthoDBiEOG092C5OQU.
PhylomeDBiO59771.

Enzyme and pathway databases

ReactomeiR-SPO-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

PROiO59771.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03172. Adenylate_kinase_UMP_CMP_kin. 1 hit.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKCY_SCHPO
AccessioniPrimary (citable) accession number: O59771
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: August 1, 1998
Last modified: September 7, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.